Q5AQA6 · LP9E_EMENI
- ProteinAA9 family lytic polysaccharide monooxygenase E
- GeneLPMO9E
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids402 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H2O2 or O2 as a cosubstrate (Probable).
Catalytic activity
Cofactor
Note: Binds 1 copper ion per subunit.
Biotechnology
Lignocellulose is the most abundant polymeric composite on Earth and is a recalcitrant but promising renewable substrate for industrial biotechnology applications. Together with cellobiose dehydrogenases (CDHs) an enzymatic system capable of oxidative cellulose cleavage is formed, which increases the efficiency of cellulases and put LPMOs at focus of biofuel research.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 17 | Cu2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 102 | Cu2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 180 | O2 (UniProtKB | ChEBI) | |||
Binding site | 189 | O2 (UniProtKB | ChEBI) | |||
Binding site | 191 | Cu2+ (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | cellulase activity | |
Molecular Function | cellulose binding | |
Molecular Function | metal ion binding | |
Molecular Function | monooxygenase activity | |
Biological Process | cellulose catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAA9 family lytic polysaccharide monooxygenase E
- EC number
- Short namesLPMO9E
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionQ5AQA6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-16 | ||||
Chain | PRO_5010179224 | 17-402 | AA9 family lytic polysaccharide monooxygenase E | ||
Disulfide bond | 72↔194 | ||||
Glycosylation | 75 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 113↔117 | ||||
Glycosylation | 154 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 364-400 | CBM1 | |||
Domain
Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence similarities
Belongs to the polysaccharide monooxygenase AA9 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length402
- Mass (Da)40,494
- Last updated2005-04-26 v1
- Checksum8A71FE2F40F9D6E7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BN001306 EMBL· GenBank· DDBJ | CBF83171.1 EMBL· GenBank· DDBJ | Genomic DNA |